Literature summary for 3.5.1.30 extracted from

Li, Z.; Xu, J.; Jiang, T.; Ge, Y.; Liu, P.; Zhang, M.; Su, Z.; Gao, C.; Ma, C.; Xu, P.
Overexpression of transport proteins improves the production of 5-aminovalerate from L-lysine in Escherichia coli (2016), Sci. Rep., 6, 30884 .

Search for more literature for 3.5.1.30

Application

Application	Comment	Organism
synthesis	the enzyme is useful to produce the nylon-5 monomer 5-aminovalerate from L-lysine in large scale	Pseudomonas putida
synthesis	2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are coexpressed in Escherichia coli BL21(DE3) to produce nylon-5 monomer 5-aminovalerate from L-lysine. PP2911 (4-aminobutyrate transporter in Pseudomonas putida) and LysP (the lysine specific permease in Escherichia coli) are overexpressed to promote 5-aminovalerate production using whole cells of recombinant Escherichia coli. The constructed Escherichia coli strain overexpressing transport proteins exhibits good 5-aminovalerate production performance and might serve as a promising biocatalyst for 5-aminovalerate production from L-lysine. This strategy not only shows an efficient process for the production of nylon monomers but also might be used in production of other chemicals	Pseudomonas putida

Cloned(Commentary)

Cloned (Comment)	Organism
2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are coexpressed in Escherichia coli BL21(DE3) to produce nylon-5 monomer 5-aminovalerate from L-lysine	Pseudomonas putida
gene davA, coexpression with gene davB from construct pETDuet-DavAB in Escherichia coli strain BL21(DE3)	Pseudomonas putida

Protein Variants

Protein Variants	Comment	Organism
additional information	lysine 2-monooxygenase (DavB) and delta-aminovaleramidase (DavA) are co-expressed in Escherichia coli BL21(DE3) to produce nylon-5 monomer 5-aminovalerate from L-lysine. Then, PP2911 (4-aminobutyrate transporter in Pseudomonas putida) and LysP (the lysine specific permease in Escherichia coli) are overexpressed to promote 5-aminovalerate production using whole cells of recombinant Escherichia coli, strain optimization for large scale production, overview. Overexpression of transport proteins improves the production of 5-aminovalerate from L-lysine in Escherichia coli. The optimum catalytic conditions are determined to be reaction temperature 30°C, substrate concentration 40 g/l, and biocatalyst concentration 60 OD600nm	Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5-aminopentanamide + H2O	Pseudomonas putida	-	5-aminopentanoate + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	Q88QV2	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5-aminopentanamide + H2O	-	Pseudomonas putida	5-aminopentanoate + NH3	-	?

Synonyms

Synonyms	Comment	Organism
DavA	-	Pseudomonas putida
delta-aminovaleramidase	-	Pseudomonas putida

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	in vivo activity	Pseudomonas putida

General Information

General Information	Comment	Organism
metabolism	5-aminovalerate, produced by the enzyme DavA, is an intermediate of L-lysine catabolism that is called aminovalerate pathway in Pseudomonas putida	Pseudomonas putida

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Release 2023.1 (January 2023)